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Articles by Anna Seelig
Pressure Protein Denaturation Compared to Thermal and Chemical Unfolding: Analyses with Cooperative Models
Introduction Click to copy section linkSection link copied! Proteins can be inactivated or unfolded by heating, (1−5) chemical agents, (6−8) or high pressure. (9,10) Unfolding has been monitored by various spectroscoptic techniques that reveal structural changes. Quantitative thermodynamic information in terms of the heat capacity change, cp(T), has been gained by differential scanning calorimetry (DSC).
Pressure Protein Denaturation Compared to Thermal and Chemical Unfolding: Analyses with Cooperative Models
Introduction Click to copy section linkSection link copied! Proteins can be inactivated or unfolded by heating, (1−5) chemical agents, (6−8) or high pressure. (9,10) Unfolding has been monitored by various spectroscoptic techniques that reveal structural changes. Quantitative thermodynamic information in terms of the heat capacity change, cp(T), has been gained by differential scanning calorimetry (DSC).
Pressure protein denaturation compared to thermal and chemical unfolding - Analyses with cooperative models
Abstract The thermodynamics of pressure induced protein unfolding (denaturation) could so far not be directly compared with protein unfolding induced by temperature or chemical agents. Here we provide a new cooperative model for pressure induced protein denaturation, that allows the quantitative comparison of the three denaturing processes based on their free energy, enthalpy, entropy, and cooperativity. As model proteins we use apolipoprotein A-1 and lysozyme.
Chemical Protein Unfolding - A Simple Cooperative Model
30 Volume Changes Associated with Guanidine Hydrochloride, Temperature, and Ethanol Induced Unfolding of Lysozyme Sirotkin, Vladimir A.; Winter, Roland Journal of Physical Chemistry B (2010), 114 (50), 16881-16886CODEN: JPCBFK; ISSN:1520-6106. (American Chemical Society) We studied the guanidine hydrochloride (GdnHCl)-, temp.-, and ethanol-induced unfolding of lysozyme using high-precision densitometric measurements, aiming to characterize and compare the vol.
Chemical protein unfolding - A simple cooperative model
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Protein Unfolding—Thermodynamic Perspectives and Unfolding Models
Open AccessArticle by Joachim Seelig * and Anna Seelig Biozentrum, University of Basel, Spitalstrasse 41, CH-4056 Basel, Switzerland * Author to whom correspondence should be addressed. Int. J. Mol. Sci.
Molecular understanding of calorimetric protein unfolding experiments
Abstract Testing and predicting protein stability gained importance because proteins, including antibodies, became pharmacologically relevant in viral and cancer therapies. Isothermal scanning calorimetry is the principle method to study protein stability. Here, we use the excellent experimental heat capacity Cp(T) data from the literature for a critical inspection of protein unfolding as well as for the test of a new cooperative model.
How phosphorylation and ATPase activity regulate anion flux through the cystic fibrosis transmembrane conductance regulator (CFTR).
How phosphorylation and ATPase activity regulate anion flux through the cystic fibrosis transmembrane conductance regulator (CFTR). VOLUME 291 (2016) PAGES 14483–14498 A word was misspelled in the title. The correct title is shown above. © 2016 by The American Society for Biochemistry and Molecular Biology, Inc.
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